1jqc
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1jqc |SIZE=350|CAPTION= <scene name='initialview01'>1jqc</scene>, resolution 1.61Å | |PDB= 1jqc |SIZE=350|CAPTION= <scene name='initialview01'>1jqc</scene>, resolution 1.61Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jpr|1JPR]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqc OCA], [http://www.ebi.ac.uk/pdbsum/1jqc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jqc RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hogbom, M.]] | [[Category: Hogbom, M.]] | ||
[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: MN]] | ||
[[Category: mn substituted]] | [[Category: mn substituted]] | ||
[[Category: oxidized by h2o2/nh2oh]] | [[Category: oxidized by h2o2/nh2oh]] | ||
| Line 33: | Line 34: | ||
[[Category: ribonucleotide reductase r2]] | [[Category: ribonucleotide reductase r2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:37:30 2008'' |
Revision as of 18:37, 30 March 2008
| |||||||
| , resolution 1.61Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||
| Related: | 1JPR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine
Overview
The di-iron carboxylate proteins constitute a diverse class of non-heme iron enzymes performing a multitude of redox reactions. These reactions usually involve high-valent Fe-oxo species and are thought to be controlled by carboxylate shifts. Owing to their short lifetime, the intermediate structures have so far escaped structural characterization by X-ray crystallography. In an attempt to map the carboxylate conformations available to the protein during different redox states and different ligand environments, we have studied metal-substituted forms of the R2 protein of ribonucleotide reductase from Escherichia coli. In the present work we have solved the crystal structures of Mn-substituted R2 oxidized in two different ways. Oxidation was performed using either nitric oxide or a combination of hydrogen peroxide and hydroxylamine. The two structures are virtually identical, indicating that the oxidation states are the same, most likely a mixed-valent MnII-MnIII centre. One of the carboxylate ligands (D84) adopts a new, so far unseen, conformation, which could participate in the mechanism for radical generation in R2. E238 adopts a bridging-chelating conformation proposed to be important for proper O2 activation but not previously observed in the wild-type enzyme. Probable catalase activity was also observed during the oxidation with H2O2, indicating mechanistic similarities to the di-Mn catalases.
About this Structure
1JQC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation., Hogbom M, Andersson ME, Nordlund P, J Biol Inorg Chem. 2001 Mar;6(3):315-23. PMID:11315567
Page seeded by OCA on Sun Mar 30 21:37:30 2008
